RPOC_FERNB
ID RPOC_FERNB Reviewed; 1650 AA.
AC A7HNY1;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=Fnod_1781;
OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=381764;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01322};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR EMBL; CP000771; ABS61614.1; -; Genomic_DNA.
DR RefSeq; WP_011994905.1; NC_009718.1.
DR AlphaFoldDB; A7HNY1; -.
DR SMR; A7HNY1; -.
DR STRING; 381764.Fnod_1781; -.
DR PRIDE; A7HNY1; -.
DR EnsemblBacteria; ABS61614; ABS61614; Fnod_1781.
DR KEGG; fno:Fnod_1781; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002415; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 2.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 2.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1650
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353364"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 747
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 749
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 751
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1078
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1650 AA; 186750 MW; 4F43AD24E44C236A CRC64;
MSSSFKRKIA SVNVRVASPE VIRNWSNGEV KKAETINYRT FKPERDGLFC ERIFGPVKDY
ECACGKYSGK KYEGTVCEKC GVKVESKDAR RRRFGHIELA APVTHVWYLK NSPSVIATLL
DMTVKDIETI VYFGSRRVNE RVVIVTDPKN TPFIKGSILN QTEYEIYAQK WDFEVSPAYI
VKEPRSPLVS DIDGEVHIKH EKTHTDRELY WIVVKNISRT ELKVYTGMVL NFKDNDQVNQ
GDEIVSEKRV EAIFAPFDGT VEVDEISETI TINPLPTSKN NPITFSLPYG VRALVKNNEK
VKKGQQLTTE TILNSIVAPV SGTIRYSKQL NLRPLENGLY EVLTNGVIYI ENVQNIKQYP
VFEGAPIQVE DGQMVKAGDI LADRFLFEEE KLTIEEYKLF SEYYPGMFVV EEQIENDKPI
MVITDIDPSV SEETGIKKGQ VITQQDYEAY SRIYPGKIEA ETGAMAIKKL LEKIDLEVMK
AEIEAELKKI PKSSVRAKKL LKKMKIVKDL IDSQTKPEWM VLEALPVVPP EIRPMIQIDG
GRFATTDLND LYRRVIMRNN RLKKLLEMNA PEVIVRNEKR MLQEAVDNLI FNGKIGKAYV
DRNGRQLKSL TDLIRGKKGR FRRNLLGKRV DYSGRAVIVV GPHLKIHECG LPKKMALELF
EPFVIAELSK EENTEAPQTK VKKYRKELQR EDPKAWEKLE KVIQGRVVLL NRAPTLHRMS
IQAFEPKLIE GNAIQLHPLV CPPFNADFDG DQMAVHLPLS PAAQAEARLL MLSRYNIISP
AHGKPISMPG KDIVAGVYYL TMVDKNYDKI EPENIKWKFA NPEEAELAYE FGFIKLHEPI
IIKINDKAIK TTFGRVIFNS ILPEELRDYN KTFGKNGIKD VVYKTFKTHG IDRTADLLDS
IKDLGFHYAT ISGLTISLKD FMISPKKNEI ITNAMKKIEY IEKLYDDGLL SDEEKYKETI
KIWTETTNLV QEETYRYLGE NPFNPVYIMV DSGARGNKDQ LKQLSGMRGL MADPSGRTIE
IPIISNFREG LSVLEFFIST HGARKGSADT ALRTSSAGYL TRRLVDVVQS VVVTEPDCGT
HEGVRATLLK SSDNFVVEKI EDFIFGRVLA KDIYEPGTGN ILVNPNTNKS YTRDTVILDE
DAKFLSNYKK RVNVVEESIL DLSVGNIPEV YAELAEDIDT PSGLIPSETE IDWDVVRKLR
DAGIKNVKIK LYPIVGSVIS EEIVWDKDRK KQIAVEEEQV DVALAKLLEE NNIDSVYVRP
EIYVRSVLTC ESEHGVCAKC YGLDLSNHKV VTVGESVGII AAQSIGEPGT QLTMRTFHTG
GIATTADITQ GLPRVEELFE ARKKTKDPEG IFSKVKGTVV DISNDEPKKI YIQDELGGIH
EYEVPSRVRV NVTVGQKVLP GQSLTSGSLK VRKILEELGP EETATYLLKE IKRVYVQQGV
DIHDKHFELI IRQMLNKAEV IDSGDTEFLP GDLVPISLLN KVNREIMEGN AKVEMNRKKI
IGRELAKHII VKNEDGEIVE LAAEGEEVTE ELLEKLIEYG IKEVVIMNHD KEKEVYQILP
KETVKYRRRL LRITQASLEY EGWLSAASFQ QTQQVLTDAA IKGAVDYLKG LKENVIVGQL
IPAGTGFDIF SSVQYEETPR LAKEEKEKFA
